ID A0A2V1DXH4_9PLEO Unreviewed; 2180 AA.
AC A0A2V1DXH4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Putative polyketide synthase {ECO:0000313|EMBL:PVI03058.1};
GN ORFNames=DM02DRAFT_698803 {ECO:0000313|EMBL:PVI03058.1};
OS Periconia macrospinosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Periconiaceae; Periconia.
OX NCBI_TaxID=97972 {ECO:0000313|EMBL:PVI03058.1, ECO:0000313|Proteomes:UP000244855};
RN [1] {ECO:0000313|EMBL:PVI03058.1, ECO:0000313|Proteomes:UP000244855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSE2036 {ECO:0000313|EMBL:PVI03058.1,
RC ECO:0000313|Proteomes:UP000244855};
RX PubMed=29679020; DOI=10.1038/s41598-018-24686-4;
RA Knapp D.G., Nemeth J.B., Barry K., Hainaut M., Henrissat B., Johnson J.,
RA Kuo A., Lim J.H.P., Lipzen A., Nolan M., Ohm R.A., Tamas L.,
RA Grigoriev I.V., Spatafora J.W., Nagy L.G., Kovacs G.M.;
RT "Comparative genomics provides insights into the lifestyle and reveals
RT functional heterogeneity of dark septate endophytic fungi.";
RL Sci. Rep. 8:6321-6321(2018).
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DR EMBL; KZ805335; PVI03058.1; -; Genomic_DNA.
DR STRING; 97972.A0A2V1DXH4; -.
DR Proteomes; UP000244855; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.11460; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF13; POLYKETIDE SYNTHASE 1; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000244855};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..423
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2094..2171
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2180 AA; 238352 MW; 1CBAEC850A3777C0 CRC64;
MPIAIIGISV RAGSAATPDE FFEMLSRGRS AFSPEIPTDR FNNASFYHPN PGKLGCINTN
GASFIQQDIT KFDAPFFSIT ELEATSMDPQ QRLLLECAFE ALDNAGIQKH TTVGKDIGVF
MGAGSPEYEV DLFRDSDTMP MFQATGNHLA MQSNRISHFF DWRGPSVTMD TACSSSLTAV
HFACQSIRNR ESEIALVGGC NLNLIPEYFI NYSTSRLMGN DGRSYSFDER GTGYGRGEGC
GMLLLKPLDQ ALKDNDYVRA VISASGVNQD GYTPGITMPN GESQETLMRK VYHDAGLDPA
QTGYVEAHGT GTRVGDPIEV TALHNVFNGR SLRNPLYLGS VKSNIGHLES ASGILAVIKV
AVGLDRRFIL PNYDFKKGNP KIPFAEWGLK VPIRQVLWPK GKRYASINNF GFGGSNAHLV
MERAPMRITG GAVSLLKQDP TKKLFVFSAA DKTACQKIMS NLVVYLEQRP EMFQRDLMSN
VAYTLGQRRS LMPWRVAIPA KEAFDLSTKI TMGNFNPVKE TGAPRIGFVC TGQGAQWWAM
GRELYESYPI FTQTIDKADA ILTSLGAPYS LVDELGRDEK MTQINQAHIS QPACTAIQLA
LIELLRSWGV TPTAVVGHSS GEIAAAFAAG ILSFDSAMQI AYHRGRLVPV LKERHPDLQG
TMMAIGCGKE EIDPLLEQLT QREVRIACYN SPESLTMSGD TPAIAELQQI LEDQQIFNRR
LVIETAYHSH HMELIAEDYF ASIKELPSPD KTDVRFFSSL TGKEAVHSEL ESNYWVRNLT
HPVKFSQAFT HLVSPTGDFS TGVDMIVEIG PHSAMQGPVK QILNAAGGAA VKIPYTTCLA
RKKDAVDTML DLASKLFCKG TPVDLASVNF PKMVKKPSLL IDLPRYPWNH TTTYWHESRI
AKLHKHRSFP RHDILGTLSN YSNDLEPIWR NIVRLDDLPW LRHHKIQSLT IFPISGFVGM
AIEAATQHAQ SKDIAIGQVE LHDVNVNTPL MLPDEDVEMT ITLRSPQFAD VGLAKITSKF
LIHSYLAGKG WTENCTGTVT VKSNELNEVD GQRQFEHKSS SIAHQIAAIE KAETLVPQEQ
IYDALEKMGV SYGSVFQGLT ECRADDKRAA ANITVTDTAA DMPEHFETKH IVHPAFLEQL
IQMYWPILGA GRSSLNVVCL PASIGKLTVS WKVLEQAKAP GQSLRAYSVA HKPLSVQKPS
KVSMFAAANG ETLIEIDDLT IAPLPADEVD GDVQAARELC FKQIWEPILA PLDLDEEIRV
DSPQADGMSN GTATPNTPIC IIHGSSSAQV ELARMLAASI ESLNNAKVDM GLLEEIDATD
KQLICITELD EFILPTLTPA QFKALQTIVE NSDGMLWVTR GAYGQAADPT GNMVVGLSRA
IRSENMYKFA NLDLDAEERL EDSAAIRAIL KVFKTVMSAA NVENVEMEFQ ERQGAFLTPR
IVQDEVINDY VHKRTFPPAV EENKFGGSSR SLRMAIQNPG MLGSIFFTDD ELRKQPLGSD
EIEILVKAVA LNSRDVEVAM GHIEATGFGE ECSGIVTAVG NDVKAFAVGD RVAAIAGGAF
ATYVRAKADF ALKLSSKISF EDAAGLPLAQ CSAHYALIEL GRLEDDETVL VLNGAGAAGQ
AAVSLAQTLG STVFATVATV EDKQILMDAY DLPEDYIFYS GDEQLASSIR RTTNGRGVDV
VFSVHATTSC IQSALECIAE FGRFVRAEVN DPSSKLKLDK SSFSFLSFDI HNLATHKPRA
VRRLIKDVNR SFKYGKLRTT EGATIVSLAE IAKAFKAARS SPSSNRTIVL PGPDDLVKMT
PSKEVVKLFK ENATYILIGG TGGLGRGMTR WMATKGARTV VLISRSGSAT GQVKTLVDDM
ALLGVDVVVH SCNVVNRDEV DALLEKIAHL PPIRGVIHTA MVLRDKMFAK MTPTDWIEIT
ENKVHGAWNF HNALLSTPLD LFILYSSCAA AMGGRGQTAY AAANIFMDAF AQYRRSLGLP
GASLGPAAVL DSGYLSENLD LYDEIARNIG DNYIRESEVL SLLESCLDGT AESSCNNHII
TGVKLDPMKM QFWATDAKYR DMRLAAEAIA AQNNHGSKTV SWNAAVKAAA SLLEAEQVVC
DGLTDKIAKT LGLELEEVDP TRNLSNYALD SLTAIDVRNF ITREFESTMQ VLEVLASGTI
QTLAKAVCAK SKLLKSLTFR
//
